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Literature summary for 2.3.1.157 extracted from

  • Olsen, L.R.; Roderick, S.L.
    Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites (2001), Biochemistry, 40, 1913-1921.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method. X-ray crystal structure of the bifunctional enzyme in complex with UDP-GlcNAc and CoA, determined to 2.1 A resolution and reveals a two-domain architecture that is responsible for the two reactions of EC 2.3.1.157 and EC 2.7.7.23. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-phosphate to GlcNAc-1-phosphate and displays the longest left-handed parallel alpha-helix observed to date. The acetyltransferase active site defined by the binding site for CoA makes use of residues from all three subunits and is positioned beneath an open cavity large enough to accommodate the Glc-1-PO4 acetyl acceptor. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-phosphate to form the final products UDP-GlcNAc and pyrophosphate Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucosamine 1-phosphate + acetyl-CoA Escherichia coli the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine N-acetyl-D-glucosamine 1-phosphate + CoA
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Organism

Organism UniProt Comment Textmining
Escherichia coli P0ACC7
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucosamine 1-phosphate + acetyl-CoA the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine Escherichia coli N-acetyl-D-glucosamine 1-phosphate + CoA
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D-glucosamine 1-phosphate + acetyl-CoA the bifunctional enzyme also possesses the activity of EC 2.7.7.23. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-phosphate to GlcNAc-1-phosphate. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-phosphate to form the final products UDP-GlcNAc and pyrophosphate Escherichia coli N-acetyl-D-glucosamine 1-phosphate + CoA
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Synonyms

Synonyms Comment Organism
N-acetylglucosamine-1-phosphate uridyltransferase bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase Escherichia coli